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Merck

A4187

Sigma-Aldrich

Anti-Goat IgG (whole molecule)–Alkaline Phosphatase antibody produced in rabbit

affinity isolated antibody, buffered aqueous glycerol solution

Sinónimos:

Rabbit Anti-Goat IgG (whole molecule)–AP

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

conjugate

alkaline phosphatase conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

species reactivity

goat

technique(s)

direct ELISA: 1:30,000
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:50
western blot: 1:30,000

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

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General description

IgG antibodies regulate several functions such as complement activation and phagocytosis. Thus they play a crucial role in facilitating cytological immune responses. Polyclonal anti-goat IgG (whole molecule)–alkaline phosphatase antibody (diluted 1:15,000) can be used as a secondary antibody for immunoblotting of Sall4. This antibody can also be used in immunohistochemistry (diluted1:400) . Rabbit anti-goat IgG antibody reacts specifically with goat IgG and normal goat serum.
Primary goat antibodies are often used to study target proteins for various clinical and research purposes. Thus, secondary anti-goat antibody conjugated to a detectable substrate can be used to facilitate the accurate detection and localization of target proteins.

Specificity

Binds all goat Igs

Immunogen

Purified goat IgG.

Application

Anti-Goat IgG (whole molecule)-Alkaline Phosphatase antibody is suitable for use in immunoblotting. The product can also be used for direct ELISA (1:30,000) and immunohistochemistry (1:50 using formalin-fixed, paraffin-embedded sections).
Detection of TLR2 and TLR4 in protein extracts from epidermal keratinocytes was performed by western blot using alkaline phosphatase conjugated rabbit anti-goat IgG as the secondary at a 1:2500 dilution.

Physical form

Solution in 0.05 M Tris buffer, pH 8.0, containing 1 mM MgCl2, 1% bovine serum albumin, 50% glycerol and 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 2


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C Fajardo-Lira et al.
Journal of dairy science, 83(10), 2190-2199 (2000-10-26)
In the present study, we investigated the effect of Pseudomonas spp. growth on the plasmin enzymatic system in casein and whey fractions of fresh milk. Two bacterial strains, Pseudomonas spp. SRM28A and Pseudomonas fluorescens M3/6, were inoculated at a level
Andor Pivarcsi et al.
International immunology, 15(6), 721-730 (2003-05-17)
Keratinocytes have the ability to kill pathogenic fungi and bacteria by producing antimicrobial substances. Recent studies suggest that microbial components use signaling molecules of the human Toll-like receptor (TLR) family to transduce signals in various cells. Here we provide evidence
Menhaj et al.
Planta, 209(4), 406-413 (1999-11-07)
An antibody was raised against the protein HL#2 which is a nuclear-encoded light-stress-induced protein of barley (Hordeum vulgare L.). The expression of the mRNA and the protein of HL#2 was determined under the influence of high light and methyl jasmonate.
L Moysset et al.
Planta, 213(4), 565-574 (2001-09-15)
The intracellular localization of phytochrome in the pulvini of Robinia pseudoacacia L. was analyzed by immunogold electron microscopy after red (R; 15 min) and far-red (FR; 5 min) irradiation 2 h after the beginning of the photoperiod. Screening of the
Gregory G Martin et al.
Archives of biochemistry and biophysics, 588, 25-32 (2015-11-07)
Both sterol carrier protein-2/sterol carrier protein-x (SCP-2/SCP-x) and liver fatty acid binding protein (L-FABP) have been proposed to function in hepatobiliary bile acid metabolism/accumulation. To begin to address this issue, the impact of ablating L-FABP (LKO) or SCP-2/SCP-x (DKO) individually

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